The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1

Ryoko Maesaki, Kentaro Ihara, Toshiyuki Shimizu, Shinya Kuroda, Kozo Kaibuchi, Toshio Hakoshima

研究成果: Article査読

137 被引用数 (Scopus)

抄録

The small G protein Rho has emerged as a key regulator of cellular events involving cytoskeletal reorganization. Here we report the 2.2 Å crystal structure of RhoA bound to an effector domain of protein kinase PKN/PRK1. The structure reveals the antiparallel coiled-coil finger (ACC finger) fold of the effector domain that binds to the Rho specificity-determining regions containing switch I, β strands B2 and B3, and the C-terminal α helix A5, predominantly by specific hydrogen bonds. The ACC finger fold is distinct from those for other small G proteins and provides evidence for the diverse ways of effector recognition. Sequence analysis based on the structure suggests that the ACC finger fold is widespread in Rho effector proteins.

本文言語English
ページ(範囲)793-803
ページ数11
ジャーナルMolecular Cell
4
5
DOI
出版ステータスPublished - 11-1999
外部発表はい

All Science Journal Classification (ASJC) codes

  • 分子生物学
  • 細胞生物学

フィンガープリント

「The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル